1xvo
From Proteopedia
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|PDB= 1xvo |SIZE=350|CAPTION= <scene name='initialview01'>1xvo</scene>, resolution 0.84Å | |PDB= 1xvo |SIZE=350|CAPTION= <scene name='initialview01'>1xvo</scene>, resolution 0.84Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1xvm|1XVM]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xvo OCA], [http://www.ebi.ac.uk/pdbsum/1xvo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xvo RCSB]</span> | ||
}} | }} | ||
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[[Category: Lamzin, V S.]] | [[Category: Lamzin, V S.]] | ||
[[Category: Schmidt, A.]] | [[Category: Schmidt, A.]] | ||
| - | [[Category: SO4]] | ||
[[Category: atomic resolution]] | [[Category: atomic resolution]] | ||
[[Category: trypsin]] | [[Category: trypsin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:55:17 2008'' |
Revision as of 21:55, 30 March 2008
| |||||||
| , resolution 0.84Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Related: | 1XVM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Trypsin from Fusarium oxysporum at pH 6
Overview
The analysis of anisotropic atomic displacement parameters for the direct extraction of functionally relevant motion from X-ray crystal structures of Fusarium oxysporum trypsin is presented. Several atomic resolution structures complexed with inhibitors or substrates and determined at different pH values and temperatures were investigated. The analysis revealed a breathing-like molecular motion conserved across trypsin structures from two organisms and three different crystal forms. Directional motion was observed suggesting a change of the width of the substrate-binding cleft and a change in the length of the specificity pocket. The differences in direction of motion across the structures are dependent on the mode of substrate or inhibitor binding and the chemical environment around the active-site residues. Together with the occurrence of multiple-residue conformers, they reflect spatial rearrangement throughout the deacylation pathway.
About this Structure
1XVO is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.
Reference
Extraction of functional motion in trypsin crystal structures., Schmidt A, Lamzin VS, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1132-9. Epub 2005, Jul 20. PMID:16041079
Page seeded by OCA on Mon Mar 31 00:55:17 2008
